PUBLICATION

Variants in the Oxidoreductase PYROXD1 Cause Early-Onset Myopathy with Internalized Nuclei and Myofibrillar Disorganization

Authors
O'Grady, G.L., Best, H.A., Sztal, T.E., Schartner, V., Sanjuan-Vazquez, M., Donkervoort, S., Abath Neto, O., Sutton, R.B., Ilkovski, B., Romero, N.B., Stojkovic, T., Dastgir, J., Waddell, L.B., Boland, A., Hu, Y., Williams, C., Ruparelia, A.A., Maisonobe, T., Peduto, A.J., Reddel, S.W., Lek, M., Tukiainen, T., Cummings, B.B., Joshi, H., Nectoux, J., Brammah, S., Deleuze, J.F., Ing, V.O., Ramm, G., Ardicli, D., Nowak, K.J., Talim, B., Topaloglu, H., Laing, N.G., North, K.N., MacArthur, D.G., Friant, S., Clarke, N.F., Bryson-Richardson, R.J., Bönnemann, C.G., Laporte, J., Cooper, S.T.
ID
ZDB-PUB-161018-3
Date
2016
Source
American journal of human genetics   99(5): 1086-1105 (Journal)
Registered Authors
Bryson-Richardson, Robert, Ruparelia, Avnika, Sztal, Tamar Esther
Keywords
none
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cell Nucleus/genetics*
  • Cell Nucleus/metabolism
  • Chlorocebus aethiops
  • Cohort Studies
  • Creatine Kinase/genetics
  • Creatine Kinase/metabolism
  • Cytoplasm/metabolism
  • Distal Myopathies/genetics*
  • Distal Myopathies/pathology
  • ELAV-Like Protein 4/genetics
  • ELAV-Like Protein 4/metabolism
  • Female
  • Flavoproteins/metabolism
  • Gene Deletion
  • Genetic Variation*
  • Genome-Wide Association Study
  • Glutathione Reductase/genetics
  • Glutathione Reductase/metabolism
  • HEK293 Cells
  • Humans
  • Male
  • Muscle, Skeletal/pathology
  • Mutation, Missense
  • Myopathies, Structural, Congenital/genetics*
  • Myopathies, Structural, Congenital/pathology
  • Oxidoreductases/genetics*
  • Oxidoreductases/metabolism
  • Pedigree
  • Protein Conformation
  • Saccharomyces cerevisiae Proteins/genetics
  • Saccharomyces cerevisiae Proteins/metabolism
  • Zebrafish/genetics
PubMed
27745833 Full text @ Am. J. Hum. Genet.
Abstract
This study establishes PYROXD1 variants as a cause of early-onset myopathy and uses biospecimens and cell lines, yeast, and zebrafish models to elucidate the fundamental role of PYROXD1 in skeletal muscle. Exome sequencing identified recessive variants in PYROXD1 in nine probands from five families. Affected individuals presented in infancy or childhood with slowly progressive proximal and distal weakness, facial weakness, nasal speech, swallowing difficulties, and normal to moderately elevated creatine kinase. Distinctive histopathology showed abundant internalized nuclei, myofibrillar disorganization, desmin-positive inclusions, and thickened Z-bands. PYROXD1 is a nuclear-cytoplasmic pyridine nucleotide-disulphide reductase (PNDR). PNDRs are flavoproteins (FAD-binding) and catalyze pyridine-nucleotide-dependent (NAD/NADH) reduction of thiol residues in other proteins. Complementation experiments in yeast lacking glutathione reductase glr1 show that human PYROXD1 has reductase activity that is strongly impaired by the disease-associated missense mutations. Immunolocalization studies in human muscle and zebrafish myofibers demonstrate that PYROXD1 localizes to the nucleus and to striated sarcomeric compartments. Zebrafish with ryroxD1 knock-down recapitulate features of PYROXD1 myopathy with sarcomeric disorganization, myofibrillar aggregates, and marked swimming defect. We characterize variants in the oxidoreductase PYROXD1 as a cause of early-onset myopathy with distinctive histopathology and introduce altered redox regulation as a primary cause of congenital muscle disease.
Genes / Markers
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping